Using a model protein with a 40 residue hydrophobic transmembrane segment, we have measured the ability of all the 20 naturally occurring amino acids to form a tight turn when placed in the middle of the hydrophobic segment. Turn propensities in a transmembrane helix are found to be markedly different from those of globular proteins, and in most cases correlate closely with the hydrophobicity of the residue. The turn propensity scale may be used to improve current methods for membrane protein topology prediction.

A turn propensity scale for transmembrane helices.

MONNE', MAGNUS LUDVIG;
1999-01-01

Abstract

Using a model protein with a 40 residue hydrophobic transmembrane segment, we have measured the ability of all the 20 naturally occurring amino acids to form a tight turn when placed in the middle of the hydrophobic segment. Turn propensities in a transmembrane helix are found to be markedly different from those of globular proteins, and in most cases correlate closely with the hydrophobicity of the residue. The turn propensity scale may be used to improve current methods for membrane protein topology prediction.
1999
File in questo prodotto:
File Dimensione Formato  
Monne_1999.pdf

accesso aperto

Descrizione: Full_Text
Tipologia: Documento in Post-print
Licenza: DRM non definito
Dimensione 166.16 kB
Formato Adobe PDF
166.16 kB Adobe PDF Visualizza/Apri

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11563/8636
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 84
  • ???jsp.display-item.citation.isi??? 79
social impact